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Structural Transitions upon Ligand Binding in a Cooperative Dimeric Hemoglobin

William E. Royer, Jr., Wayne A. Hendrickson and Emilia Chiancone
Science
New Series, Vol. 249, No. 4968 (Aug. 3, 1990), pp. 518-521
Stable URL: http://www.jstor.org/stable/2874492
Page Count: 4
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Abstract

Comparison of the 2.4 angstrom resolution crystal structures of dimeric clam hemoglobin in the deoxygenated and carbon-monoxide liganded states shows how radically different the structural basis for cooperative oxygen binding is from that operative in mammalian hemoglobins. Heme groups are in direct communication across a novel subunit interface formed by the E and F helices. The conformational changes at this interface that accompany ligand binding are more dramatic at a tertiary level but more subtle at a quaternary level than those in mammalian hemoglobins. These findings suggest a cooperative mechanism that links ligation at one subunit with potentiation of affinity at the second subunit.

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